1E8F
STRUCTURE OF THE H61T MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN THE APO FORM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004458 | molecular_function | D-lactate dehydrogenase (cytochrome) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005777 | cellular_component | peroxisome |
| A | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| A | 0015945 | biological_process | methanol metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018465 | molecular_function | vanillyl-alcohol oxidase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
| A | 1903457 | biological_process | lactate catabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004458 | molecular_function | D-lactate dehydrogenase (cytochrome) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005777 | cellular_component | peroxisome |
| B | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| B | 0015945 | biological_process | methanol metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018465 | molecular_function | vanillyl-alcohol oxidase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
| B | 1903457 | biological_process | lactate catabolic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 410 |
| Details | Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for the catalytic mechanism; Involved in substrate deprotonation"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Tele-8alpha-FAD histidine"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1vao |
| Chain | Residue | Details |
| A | ARG504 | |
| A | HIS422 | |
| A | TYR503 | |
| A | ASP170 | |
| A | TYR108 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1vao |
| Chain | Residue | Details |
| B | ARG504 | |
| B | HIS422 | |
| B | TYR503 | |
| B | ASP170 | |
| B | TYR108 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 103 |
| Chain | Residue | Details |
| A | TYR108 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP170 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | HIS422 | activator, covalently attached, increase redox potential |
| A | TYR503 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG504 | activator, electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 103 |
| Chain | Residue | Details |
| B | TYR108 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP170 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | HIS422 | activator, covalently attached, increase redox potential |
| B | TYR503 | electrostatic stabiliser, hydrogen bond donor |
| B | ARG504 | activator, electrostatic stabiliser, hydrogen bond donor |
